RPOB_ANASK
ID RPOB_ANASK Reviewed; 1422 AA.
AC B4UDT2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; OrderedLocusNames=AnaeK_2271;
OS Anaeromyxobacter sp. (strain K).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC unclassified Anaeromyxobacter.
OX NCBI_TaxID=447217;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikiva G.,
RA Beliaev A.;
RT "Complete sequence of Anaeromyxobacter sp. K.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01321};
CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC and 1 omega subunit. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR EMBL; CP001131; ACG73498.1; -; Genomic_DNA.
DR RefSeq; WP_012526295.1; NC_011145.1.
DR AlphaFoldDB; B4UDT2; -.
DR SMR; B4UDT2; -.
DR EnsemblBacteria; ACG73498; ACG73498; AnaeK_2271.
DR KEGG; ank:AnaeK_2271; -.
DR HOGENOM; CLU_000524_4_3_7; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001871; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.30.150.10; -; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
DR InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR010243; RNA_pol_bsu_bac.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 2.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR TIGRFAMs; TIGR02013; rpoB; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW Transferase.
FT CHAIN 1..1422
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141656"
FT REGION 1392..1422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1422 AA; 159061 MW; 5A118FCA30FBF0D8 CRC64;
MATTIQNNFR IRRNFGKINK IAEIPNLIAI QKFSYDKFLQ ADVPPEKRDD TGLQGVFKSV
FPIKDFNETS SLEFVSYHLE KPKYDVDECH QRGMTYSAPI KVVVRLVVWD KDEETGAQSI
RDVKEQEVYF GEIPLMTENG TFIINGTERV VVSQLHRSPG AFFDHDKGKS HSSGKLLYNA
RIIPYRGSWI DFEFDHKDIL YVRIDRRRKL PATVLLRALG ATPDTAKKDP VEFHGSAEEI
LKYYYDTETI RIEGKGKYEK DLVPDLLKGQ RATRDIRDPK SNEVIVKKNR KYTESAIKKL
VAAKMKSLPV EPEEVYTKIS AEDVVDETTG EVLLEVNEEV TEAKVEELRK RNINEFKVLF
IDNLNILPAL RDTLMQDKIS TPEEAIMEIY RRLRPGDPPT PETATNLFVN LFFNAERYDL
SKVGRLKLNY KFGIEEPLEN TVLTKRDILE VVRFLIDLKN GKPNKDVDDI DHLGNRRVRA
VGELLENQYR IGLVRMERAI KERMSLQEIE TLMPHDLINA KPVTAVIKEF FGSSQLSQFM
DQTNPLSEVT HKRRLSALGP GGLTRERAGF EVRDVHSTHY GRICPIETPE GPNIGLIASL
STYARVNEYG FVETPYRKVE KGRVTDEVTF YSALEEEKHI IAQANAPVDK KGNFTEAKVW
CRKEGEYIYV RPDEVDLMDV SPNQLVSVAA SLVPFLENDD ANRALMGSNM QRQAVPLLRT
QAPLVGTGIE AIVARDSGVT TVAKRDGVVQ SVDASRIVVK ADVPTSATDV ANEVDIYNLI
KYQRSNQNTC INQKPIVKPG ERVKKGDVIA DGPATEMGEL ALGQNVVVAF MPWQGYNFED
SILLSERLIK EDVFTSVHIE EFECVARDTK LGKEEITRDI PNVGEEALKD LDESGIIRIG
AEVKPGDILV GKITPKGETQ LSPEEKLLRA IFGEKAGDVR DSSLRVPPGV SGTVINAKVF
SRKGVEKDER AKAIEEMEEA KLLKDQNDEI KIIQDSAFQK IRRLLLGKEV TARLVDDKGE
QLLKKGDVLD DALLDTVPQR YWGEIAVAGD VQDLARKIIE NFEEQKELVK LLFGEKIGRL
KKGDELPPGV IKMVKVYVAI KRKLAVGDKM AGRHGNKGVV SRVLPEEDLP YLEDGTPVDI
VLNPLGVPSR MNVGQILETH LGWAARNVGL RLQEMIEKEW GADPLRKKLK AAFAGTEGGP
VGERLAALIE DVPEKELPKL VQKLRRGMHV ATPVFDGARE DEMKALMEEG SATLQSILFD
GRTGEPFDQD VTVGVMYMLK LHHLVDEKIH ARSIGPYSLV TQQPLGGKAQ FGGQRLGEME
VWAMEAYGAA YSLQEFLTVK SDDVVGRTRM YEAIVKGENT LESGLPESFN VLIKELQSLA
LDVELLETPE AQAAREAAER DLGGGPLGAP RGAVASGEKS SA
